Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Enantioselective Determination of Carnitine Enantiomers in Food and Supplement Samples by Chiral Liquid Chromatography-Tandem Mass Spectrometry.

Mass spectrometry (Tokyo, Japan)·2026
Same author

Identification of 2'-deoxyguanosine for an α-amylase inhibitor in the extracts of the earthworm Eisenia fetida and characterization of its inhibitory activity against porcine pancreatic α-amylase.

Enzyme and microbial technology·2025
Same author

Development of a mertansine-specific DNA aptamer and novel high-throughput sandwich enzyme-linked oligonucleotide assay for quantification and characterization of trastuzumab emtansine.

Biosensors & bioelectronics·2025
Same author

Achieving unprecedented stability in lyophilized recombinase polymerase amplification with thermostable pyruvate kinase from Thermotoga maritima.

Journal of bioscience and bioengineering·2024
Same author

Increase in the solubility of uvsY using a site saturation mutagenesis library for application in a lyophilized reagent for recombinase polymerase amplification.

Molecular biology reports·2024
Same author

Application of recombinant human pyruvate kinase in recombinase polymerase amplification.

Journal of bioscience and bioengineering·2023

Related Experiment Video

Updated: May 31, 2026

Detection of Protease Activity by Fluorescent Peptide Zymography
09:56

Detection of Protease Activity by Fluorescent Peptide Zymography

Published on: January 20, 2019

Activation of matriptase zymogen.

Kenji Kojima, Kuniyo Inouye

    Journal of Biochemistry
    |July 9, 2011
    PubMed
    Summary

    Mildly acidic pH and low ionic strength activate matriptase zymogen, a key protease in epithelial integrity. This finding is crucial for understanding protease cascade regulation in cell surface microenvironments.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Dermatology

    Background:

    • Matriptase is a type II transmembrane serine protease abundant in epithelial cells and keratinocytes.
    • It is critical for maintaining epithelial integrity and acts upstream in cellular protease cascades.
    • Zymogen activation is a key regulatory step for downstream protease activity.

    Purpose of the Study:

    • To investigate the environmental factors influencing matriptase zymogen activation.
    • To understand the role of pH and ionic strength in regulating matriptase activity.

    Main Methods:

    • Exposure of matriptase-expressing epithelial cells and homogenates to varying pH levels.
    • Assessment of matriptase zymogen activation under different ionic strength conditions.

    More Related Videos

    Detection of Functional Matrix Metalloproteinases by Zymography
    09:30

    Detection of Functional Matrix Metalloproteinases by Zymography

    Published on: November 8, 2010

    Related Experiment Videos

    Last Updated: May 31, 2026

    Detection of Protease Activity by Fluorescent Peptide Zymography
    09:56

    Detection of Protease Activity by Fluorescent Peptide Zymography

    Published on: January 20, 2019

    Detection of Functional Matrix Metalloproteinases by Zymography
    09:30

    Detection of Functional Matrix Metalloproteinases by Zymography

    Published on: November 8, 2010

    Main Results:

    • Mildly acidic pH rapidly activates matriptase zymogen.
    • High ionic strength inhibits matriptase zymogen activation.
    • Acidification and reduced ionic strength in cell-surface microenvironments are proposed triggers.

    Conclusions:

    • Environmental factors like pH and ionic strength significantly regulate matriptase activation.
    • Understanding these triggers is essential for controlling protease cascade functions.
    • This research provides insights into epithelial integrity maintenance and protease regulation.